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Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH.

Journal of Molecular Biology

metabolism, Protein Structure, Secondary, Crystallization, Binding Sites, Crystallography, X-Ray, Escherichia coli, Models, Molecular, Molecular Sequence Data, NADH, NADPH Oxidoreductases, chemistry, NADP, Amino Acid Sequence, Base Sequence

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      Abstract

      The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 A resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase.

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      Journal
      10.1006/jmbi.1995.0337
      7602590

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